Circular dichroism and conformational analysis of the membrane-modifying peptide -N-t-Boc-(Aib-L-Ala)5-Gly-Ala-Aib-Pro-Ala-Aib-Aib-Glu-(OBzl)-Gln-OMe with respect to alamethicin
✍ Scribed by R. Oekonomopulos; G. Jung
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1980
- Tongue
- English
- Weight
- 665 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The conformational analysis of the CD spectrum is reported for the synthetic and membrane‐modifying nonadecapeptide analog of alamethicin N‐t‐Boc‐(Aib‐L‐Ala)~5~‐Gly‐Ala‐Aib‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐ Gln‐OMe. The CD data are evaluated according to three different methods and are discussed with respect to those obtained from natural alamethicin and suitable models such as N‐t‐Boc‐(Aib‐L‐Ala)~7~‐OPOE, fragments of the synthetic nonadecapeptide, and the hexadecapeptide N‐t‐Boc‐(Aib‐L‐Ala)~5~‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐Gln‐OMe. The synthetic nonadecapeptide with the longer helical region exhibits membrane activities comparable to those of alamethicin, whereas the hexadecapeptide with the shorter helix is inactive.